KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in Aspergillus nidulans. Issue 4 (11th April 2015)
- Record Type:
- Journal Article
- Title:
- KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in Aspergillus nidulans. Issue 4 (11th April 2015)
- Main Title:
- KdmA, a histone H3 demethylase with bipartite function, differentially regulates primary and secondary metabolism in Aspergillus nidulans
- Authors:
- Gacek‐Matthews, Agnieszka
Noble, Luke M.
Gruber, Clemens
Berger, Harald
Sulyok, Michael
Marcos, Ana T.
Strauss, Joseph
Andrianopoulos, Alex - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p> <italic>A</italic> <italic>spergillus nidulans kdmA</italic> encodes a member of the KDM4 family of jumonji histone demethylase proteins, highly similar to metazoan orthologues both within functional domains and in domain architecture. This family of proteins exhibits demethylase activity towards lysines 9 and 36 of histone H3 and plays a prominent role in gene expression and chromosome structure in many species. Mass spectrometry mapping of <italic>A</italic><italic>. nidulans</italic> histones revealed that around 3% of bulk histone H3 carried trimethylated H3K9 (H3K9me3) but more than 90% of histones carried either H3K36me2 or H3K36me3. KdmA functions as H3K36me3 demethylase and has roles in transcriptional regulation. Genetic manipulation of KdmA levels is tolerated without obvious effect in most conditions, but strong phenotypes are evident under various conditions of stress. Transcriptome analysis revealed that – in submerged early and late cultures – between 25% and 30% of the genome is under KdmA influence respectively. Transcriptional imbalance in the <italic>kdm</italic><italic>A</italic> deletion mutant may contribute to the lethal phenotype observed upon exposure of mutant cells to low‐density visible light on solid medium. Although KdmA acts as transcriptional co‐repressor of primary metabolism genes, it is required for full expression of several genes involved in biosynthesis of secondary<abstract abstract-type="main"> <title>Summary</title> <p> <italic>A</italic> <italic>spergillus nidulans kdmA</italic> encodes a member of the KDM4 family of jumonji histone demethylase proteins, highly similar to metazoan orthologues both within functional domains and in domain architecture. This family of proteins exhibits demethylase activity towards lysines 9 and 36 of histone H3 and plays a prominent role in gene expression and chromosome structure in many species. Mass spectrometry mapping of <italic>A</italic><italic>. nidulans</italic> histones revealed that around 3% of bulk histone H3 carried trimethylated H3K9 (H3K9me3) but more than 90% of histones carried either H3K36me2 or H3K36me3. KdmA functions as H3K36me3 demethylase and has roles in transcriptional regulation. Genetic manipulation of KdmA levels is tolerated without obvious effect in most conditions, but strong phenotypes are evident under various conditions of stress. Transcriptome analysis revealed that – in submerged early and late cultures – between 25% and 30% of the genome is under KdmA influence respectively. Transcriptional imbalance in the <italic>kdm</italic><italic>A</italic> deletion mutant may contribute to the lethal phenotype observed upon exposure of mutant cells to low‐density visible light on solid medium. Although KdmA acts as transcriptional co‐repressor of primary metabolism genes, it is required for full expression of several genes involved in biosynthesis of secondary metabolites.</p> </abstract> … (more)
- Is Part Of:
- Molecular microbiology. Volume 96:Issue 4(2015)
- Journal:
- Molecular microbiology
- Issue:
- Volume 96:Issue 4(2015)
- Issue Display:
- Volume 96, Issue 4 (2015)
- Year:
- 2015
- Volume:
- 96
- Issue:
- 4
- Issue Sort Value:
- 2015-0096-0004-0000
- Page Start:
- 839
- Page End:
- 860
- Publication Date:
- 2015-04-11
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.12977 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3251.xml